ASTB_CHRVO
ID ASTB_CHRVO Reviewed; 448 AA.
AC Q7NXX6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=N-succinylarginine dihydrolase {ECO:0000255|HAMAP-Rule:MF_01172};
DE EC=3.5.3.23 {ECO:0000255|HAMAP-Rule:MF_01172};
GN Name=astB {ECO:0000255|HAMAP-Rule:MF_01172}; OrderedLocusNames=CV_1500;
OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS 12614 / NCIMB 9131 / NCTC 9757).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=243365;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC 9757;
RX PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T.,
RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R.,
RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F.,
RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S.,
RA Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M.,
RA Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P.,
RA Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S.,
RA Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N.,
RA Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P.,
RA Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R.,
RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J.,
RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F.,
RA Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z.,
RA de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F.,
RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C.,
RA Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M.,
RA Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT "The complete genome sequence of Chromobacterium violaceum reveals
RT remarkable and exploitable bacterial adaptability.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
CC -!- FUNCTION: Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-
CC succinylornithine, ammonia and CO(2). {ECO:0000255|HAMAP-
CC Rule:MF_01172}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 H2O + N(2)-succinyl-L-arginine = CO2 + N(2)-
CC succinyl-L-ornithine + 2 NH4(+); Xref=Rhea:RHEA:19533,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:58241, ChEBI:CHEBI:58514; EC=3.5.3.23;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01172};
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC pathway; L-glutamate and succinate from L-arginine: step 2/5.
CC {ECO:0000255|HAMAP-Rule:MF_01172}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01172}.
CC -!- SIMILARITY: Belongs to the succinylarginine dihydrolase family.
CC {ECO:0000255|HAMAP-Rule:MF_01172}.
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DR EMBL; AE016825; AAQ59175.1; -; Genomic_DNA.
DR RefSeq; WP_011135052.1; NC_005085.1.
DR AlphaFoldDB; Q7NXX6; -.
DR SMR; Q7NXX6; -.
DR STRING; 243365.CV_1500; -.
DR EnsemblBacteria; AAQ59175; AAQ59175; CV_1500.
DR KEGG; cvi:CV_1500; -.
DR eggNOG; COG3724; Bacteria.
DR HOGENOM; CLU_053835_0_0_4; -.
DR OMA; TLNDWVD; -.
DR OrthoDB; 567590at2; -.
DR UniPathway; UPA00185; UER00280.
DR Proteomes; UP000001424; Chromosome.
DR GO; GO:0009015; F:N-succinylarginine dihydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019544; P:arginine catabolic process to glutamate; IEA:UniProtKB-UniRule.
DR GO; GO:0019545; P:arginine catabolic process to succinate; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.75.10.20; -; 1.
DR HAMAP; MF_01172; AstB; 1.
DR InterPro; IPR037031; AstB_sf.
DR InterPro; IPR007079; SuccinylArg_d-Hdrlase_AstB.
DR Pfam; PF04996; AstB; 1.
DR TIGRFAMs; TIGR03241; arg_catab_astB; 1.
PE 3: Inferred from homology;
KW Arginine metabolism; Hydrolase; Reference proteome.
FT CHAIN 1..448
FT /note="N-succinylarginine dihydrolase"
FT /id="PRO_0000262347"
FT ACT_SITE 174
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT ACT_SITE 250
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT ACT_SITE 371
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 19..28
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 137..138
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
SQ SEQUENCE 448 AA; 48439 MW; 0647336C3B20B513 CRC64;
MNAYEVNFDG LVGPTHNYSG LSFGNVASTS NVSAASNPKL AAKQGLQKMK ALYDLGFKQG
VLAPQERPDV ASLRRLGFGG SDAEVIARAA KEAPTILAAA TSASCMWTAN AATVSPSADT
ADGRVHFTPA NLNNKFHRSI EHPTTRRVLR AMFADETRFA VHEALPAQMH FGDEGAANHT
RFCADYGQPG VEFFVFGAAA FDMRYPKPAK FPARQTLEAS QAVARLHGLS EAGVVYAQQD
PDTIDAGVFH NDVISVGNGE VLFHHQQAFL NQADVLDEIA RKLEARGGRF TAIEVPRAEV
TVEEAVKSYL FNSQLLSKPG GKMLIVVPEE CRNSERVWSY LQKLAASGGP IDEVRVFDLK
QSMQNGGGPA CLRLRVALNQ AELAAVNPKV LMSDALFASL NGWVDRHYRD RLAPEDLADP
QLLIECRGAL DELTGILGLG SVYPFQLA
